| KUBÍČEK, Karel, Hana ČERNÁ, Peter HOLUB, Josef PASULKA, Dominika HROŠŠOVÁ, Frank LOEHR, Ctirad HOFR, Štěpánka VAŇÁČOVÁ a Richard ŠTEFL. Serine phosphorylation and proline isomerization in RNAP II CTD control recruitment of Nrd1. Genes & Development. New York: Cold Spring Harbor Laboratory Press, 2012, roč. 26, č. 17, s. 1891-1896. ISSN 0890-9369. Dostupné z: https://dx.doi.org/10.1101/gad.192781.112. |
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@article{988332,
author = {Kubíček, Karel and Černá, Hana and Holub, Peter and Pasulka, Josef and Hroššová, Dominika and Loehr, Frank and Hofr, Ctirad and Vaňáčová, Štěpánka and Štefl, Richard},
article_location = {New York},
article_number = {17},
doi = {http://dx.doi.org/10.1101/gad.192781.112},
keywords = {RNA polymerase II; CTD code; phosphorylation; proline isomerization; RNA processing and degradation; NMR spectroscopy; structure},
language = {eng},
issn = {0890-9369},
journal = {Genes & Development},
title = {Serine phosphorylation and proline isomerization in RNAP II CTD control recruitment of Nrd1},
url = {http://www.ncbi.nlm.nih.gov/pubmed/22892239},
volume = {26},
year = {2012}
}
TY - JOUR
ID - 988332
AU - Kubíček, Karel - Černá, Hana - Holub, Peter - Pasulka, Josef - Hroššová, Dominika - Loehr, Frank - Hofr, Ctirad - Vaňáčová, Štěpánka - Štefl, Richard
PY - 2012
TI - Serine phosphorylation and proline isomerization in RNAP II CTD control recruitment of Nrd1
JF - Genes & Development
VL - 26
IS - 17
SP - 1891-1896
EP - 1891-1896
PB - Cold Spring Harbor Laboratory Press
SN - 08909369
KW - RNA polymerase II
KW - CTD code
KW - phosphorylation
KW - proline isomerization
KW - RNA processing and degradation
KW - NMR spectroscopy
KW - structure
UR - http://www.ncbi.nlm.nih.gov/pubmed/22892239
L2 - http://www.ncbi.nlm.nih.gov/pubmed/22892239
N2 - Recruitment of appropriate RNA processing factors to the site of transcription is controlled by post-translational modifications of the C-terminal domain (CTD) of RNA polymerase II (RNAP II). Here, we report the solution structure of the Ser5 phosphorylated (pSer5) CTD bound to Nrd1. The structure reveals a direct recognition of pSer5 by Nrd1 that requires the cis conformation of the upstream pSer5–Pro6 peptidyl-prolyl bond of the CTD. Mutations at the complex interface diminish binding affinity and impair processing or degradation of noncoding RNAs. These findings underpin the interplay between covalent and noncovalent changes in the CTD structure that constitute the CTD code.
ER -
KUBÍČEK, Karel, Hana ČERNÁ, Peter HOLUB, Josef PASULKA, Dominika HROŠŠOVÁ, Frank LOEHR, Ctirad HOFR, Štěpánka VAŇÁČOVÁ a Richard ŠTEFL. Serine phosphorylation and proline isomerization in RNAP II CTD control recruitment of Nrd1. \textit{Genes \&{} Development}. New York: Cold Spring Harbor Laboratory Press, 2012, roč.~26, č.~17, s.~1891-1896. ISSN~0890-9369. Dostupné z: https://dx.doi.org/10.1101/gad.192781.112.
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